We propose the use of two dimensional NMR experiments, in conjunction with distance geometry calculations and computer graphics, to measure the solution structure of peptides, nucleotides, and small proteins. High resolution proton NMR spectra contain enough information, to determine molecular geometries with an accuracy of a few angstroms. The important steps to obtain this information are 1) assignment of the proton NMR signals, 2) measurement of NOE's for short distances, 3) use of paramagnetic reagents for long distances, 4) calculation of molecular coordinates from the distances using distance geometry, and 5) refinement of the molecular structure using energy calculations and interactive computer graphics. Experiments are described to improve the spectral assignment procedure and to measure a wide range of distances. These include selective isotope enrichment methods for bacterial proteins. The complications introduced by molecular motion are discussed in detail. The project is a large scale one, involving a high field NMR Spectrometer, and a dedicated computer. Because of the enormous potential of the method and the very significant effort required to bring it to fruition, we propose establishing a National Research Resource Facility.